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AP U3 T1-4 (part 2)
Enzymes
| Term | Definition |
|---|---|
| optimal conditions | the conditions (temperature and pH) that allow enzymes to function optimally (at their best) |
| enzymes | macromolecules that catalyze (speed up) reactions by lowering the activation energy; Are not consumed by the reaction, Type of protein, Enzyme names end in -ase |
| substrate | the reactant an enzyme works on |
| active site | area of the enzyme in which the substrate binds |
| induced fit | enzymes will change the shape of their active site to allow the substrate to bind better |
| enzyme-substrate complex | formed when the substrate has bound to the active site of an enzyme |
| ATP-ADP Cycle | energy from exergonic reactions in a cell can be used to "recharge" ATP from ADP by bonding a 3rd phosphate to the ADP molecule. The 3rd phosphate can be removed by hydrolysis later to power a different cellular process |
| factors that can denature enzymes | temperature, pH, chemicals (salinity) |
| denature | change the shape of an enzyme |
| Effect of temperature on enzymes | The rate of enzyme activity increases with temperature (due to collision) up to a certain point, after which the enzyme will denature |
| Effect of pH on enzymes | Enzymes function best at a specific pH. Being outside the normal pH range can cause hydrogen bonds in the enzyme to break, changing the shape of the enzyme |
| Enzyme cofactors | non protein molecules that assist enzyme function |
| Inorganic cofactors | metals that assist enzyme function |
| Holoenzyme | an enzyme bound to a cofactor |
| Coenzymes | organic cofactors (vitamins) |
| Enzyme inhibitors | reduce the activity of specific enzymes |
| Permanent inhibitors | bind to enzyme with covalent bonds preventing the enzyme from ever working again (toxins & poisons) |
| Reversible inhibitors | bind to enzyme with weak interactions (while attached enzyme cannot function, but will detach so enzyme will work again at some point) |
| Competitive inhibitors | reduce enzyme activity by blocking substrates from binding to the active site; Inhibition can be reversed with increased substrate concentrations |
| Noncompetitive inhibitors: | bind to an area other than the active site (allosteric site), which changes the shape of the active site preventing substrates from binding; Type of allosteric inhibition |
| Metabolic pathway regulation | cells control metalbolic pathways by 1) Control where and when enzymes are active and switching genes that code for enzymes on or off |
| Allosteric site | regulatory site on an enzyme that is different from the active site |
| Allosteric regulation | molecules bind (noncovalent interactions) to an allosteric site which changes the shape and function of the active site; May result in inhibition (by an inhibitor) or stimulation (by an activator) of the enzymes activity |
| Allosteric activator: | substrate binds to allosteric site and stabilizes the shape of the enzyme so that the active sites remain open |
| Allosteric inhibitor | substrate binds to allosteric site and stabilizes the enzyme shape so that the active sites are closed (inactive form) |
| Cooperativity | substrate binds to one active site (on an enzyme with more than one active site) which stabilizes the active form; Considered allosteric regulation since binding at one site changes the shape of other sites |
| Feedback inhibition | the end product of a metabolic pathway can act as an inhibitor to an early enzyme in the same pathway |
Created by:
MrsCSciencetT
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